› 1ov4

X-ray diffraction
2.7Å resolution

Crystal structure of human DHEA-ST complexed with androsterone

Released:
DOI: 10.2210/pdb1ov4/pdb
PDB entry 1ov4 coloured by chain, front view.
PDB entry 1ov4 coloured by chain, side view.
PDB entry 1ov4 coloured by chain, top view.
Source organism: Homo sapiens
Primary publication:
Identifying androsterone (ADT) as a cognate substrate for human dehydroepiandrosterone sulfotransferase (DHEA-ST) important for steroid homeostasis: structure of the enzyme-ADT complex.
Chang HJ, Shi R, Rehse P, Lin SX
J Biol Chem 279 2689-96 (2004)
PMID: 14573603

Function and Biology Details

Reactions catalysed: 
3'-phosphoadenylyl sulfate + glycolithocholate = adenosine 3',5'-bisphosphate + glycolithocholate 3-sulfate
3'-phosphoadenylyl sulfate + an alcohol = adenosine 3',5'-bisphosphate + an alkyl sulfate
Biochemical function:
Biological process:
Cellular component:
Sequence domains:
Structure domain:

Structure analysis Details

Assembly composition:
homo dimer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-170360 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Sulfotransferase 2A1 Chain: A
Molecule details ›
Chain: A
Length: 293 amino acids
Theoretical weight: 34.72 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli
UniProt:
  • Canonical: Q06520 (Residues: 2-285; Coverage: 100%)
Gene names: HST, STD, SULT2A1
Sequence domains: Sulfotransferase domain
Structure domains: P-loop containing nucleotide triphosphate hydrolases

Ligands and Environments

2 bound ligands:
Ligand SO4 1 x SO4
Ligand AOX 1 x AOX
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: NSLS BEAMLINE X8C
Spacegroup: P21212
Unit cell:
a: 75.293Å b: 129.818Å c: 44.287Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.23 0.23 0.27
Expression system: Escherichia coli

Quick links

Citations

11 review citations

The Regulation of Steroid Action by Sulfation and Desulfation.
Mueller et al. (2015)
10 more

7 mentions without citation

From Steroid and Drug Metabolism to Glycobiology, Using Sulfotransferase Structures to Understand and Tailor Function.
Pedersen et al. (2022)
6 more